› 3bg3

X-ray diffraction
2.8Å resolution

Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)

Released:
DOI: 10.2210/pdb3bg3/pdb
PDB entry 3bg3 coloured by chain, front view.
PDB entry 3bg3 coloured by chain, side view.
PDB entry 3bg3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
Xiang S, Tong L
Nat Struct Mol Biol 15 295-302 (2008)
PMID: 18297087

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145857 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate carboxylase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 718 amino acids
Theoretical weight: 78.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11498 (Residues: 482-1178; Coverage: 59%)
Gene name: PC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BTI 1 x BTI
2 bound ligands:
Ligand MN 4 x MN
Ligand PYR 4 x PYR
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 81.274Å b: 173.321Å c: 118.194Å
α: 90° β: 95.87° γ: 90°
R-values:
R R work R free
0.219 0.216 0.271
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Regulation of pyruvate metabolism and human disease.
Gray et al. (2014)
10 more

4 mentions without citation

Quaternary structure of the oxaloacetate decarboxylase membrane complex and mechanistic relationships to pyruvate carboxylases.
Balsera et al. (2011)
3 more